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The Ransey Lab explores the multifaceted roles of gap junctions—essential intercellular pores that enable direct communication, metabolic exchange, and rapid adaptation to stress. These multimeric channels are formed by connexin (Cx) proteins, which assemble into hexameric hemichannels that dock with those on adjacent cells, creating conduits for the exchange of ions and small molecules. Crucial for maintaining tissue homeostasis, mutations or abnormal expression of Cx proteins are linked to a range of diseases, including congenital deafness, epilepsy, neurodegeneration, and cancer.

With 21 human Cx isoforms expressed across various tissues, their ability to mix and match in specific configurations creates remarkable functional diversity, with each isoform hypothesized to contribute distinct properties – such as small molecule permeability, gating properties, and half-life – to the channels they form.

However, critical gaps remain in our understanding of how and which specific Cx isoforms interact to form functional channels and how mixed-isoform channels influence intercellular signaling.

To address these challenges, we employ cellular and biochemical assays, flow cytometry, confocal imaging and electrophysiology to uncover novel Cx interactions, characterize isoform-specific channel properties, and elucidate the dynamic regulation of gap junctions. Our research aims to deepen our understanding of gap junction complexity, uncovering its critical roles in cellular function and enabling us to reengineer intercellular communication to address both health and disease.